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Volumn 195, Issue 11, 2013, Pages 2550-2561

Posttranslational modification of flagellin flab in shewanella oneidensis

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FLAGELLIN; LYSINE; PROTEIN FLAB; PROTEIN PSEB; PROTEIN PSEC; SERINE; UNCLASSIFIED DRUG;

EID: 84877957233     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00015-13     Document Type: Article
Times cited : (37)

References (43)
  • 2
    • 67749133487 scopus 로고    scopus 로고
    • MotX and MotY are required for flagellar rotation in Shewanella oneidensis MR-1
    • Koerdt A, Paulick A, Mock M, Jost K, Thormann KM. 2009. MotX and MotY are required for flagellar rotation in Shewanella oneidensis MR-1. J. Bacteriol. 191:5085-5093.
    • (2009) J. Bacteriol. , vol.191 , pp. 5085-5093
    • Koerdt, A.1    Paulick, A.2    Mock, M.3    Jost, K.4    Thormann, K.M.5
  • 4
    • 79959388113 scopus 로고    scopus 로고
    • Genetic and molecular characterization of flagellar assembly in Shewanella oneidensis
    • doi:10.1371/journal.pone.0021479
    • Wu L, Wang J, Tang P, Chen H, Gao H. 2011. Genetic and molecular characterization of flagellar assembly in Shewanella oneidensis. PLoS One 6:e21479. doi:10.1371/journal.pone.0021479.
    • (2011) PLoS One , vol.6 , pp. 21479
    • Wu, L.1    Wang, J.2    Tang, P.3    Chen, H.4    Gao, H.5
  • 5
    • 44849097921 scopus 로고    scopus 로고
    • Environmental adaptation: genomic analysis of the piezotolerant and psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
    • doi:10.1371/journal.pone.0001937
    • Wang F, Wang J, Jian H, Zhang B, Li S, Wang F, Zeng X, Gao L, Bartlett DH, Yu J, Hu S, Xiao X. 2008. Environmental adaptation: genomic analysis of the piezotolerant and psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans. PLoS One 3:e1937. doi:10.1371/journal.pone.0001937.
    • (2008) PLoS One , vol.3 , pp. 1937
    • Wang, F.1    Wang, J.2    Jian, H.3    Zhang, B.4    Li, S.5    Wang, F.6    Zeng, X.7    Gao, L.8    Bartlett, D.H.9    Yu, J.10    Hu, S.11    Xiao, X.12
  • 6
    • 84855768808 scopus 로고    scopus 로고
    • Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32
    • Bubendorfer S, Held S, Windel N, Paulick A, Klingl A, Thormann KM. 2012. Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32. Mol. Microbiol. 83:335-350.
    • (2012) Mol. Microbiol. , vol.83 , pp. 335-350
    • Bubendorfer, S.1    Held, S.2    Windel, N.3    Paulick, A.4    Klingl, A.5    Thormann, K.M.6
  • 7
    • 33646014793 scopus 로고    scopus 로고
    • Variation in bacterial flagellins: from sequence to structure
    • Beatson SA, Minamino T, Pallen MJ. 2006. Variation in bacterial flagellins: from sequence to structure. Trends Microbiol. 14:151-155.
    • (2006) Trends Microbiol. , vol.14 , pp. 151-155
    • Beatson, S.A.1    Minamino, T.2    Pallen, M.J.3
  • 8
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft H, Szymanski CM. 2010. Protein glycosylation in bacteria: sweeter than ever. Nat. Rev. Microbiol. 8:765-778.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 9
    • 0014979873 scopus 로고
    • Methylation of the flagellin of Salmonella typhimurium
    • Tronick SR, Martinez RJ. 1971. Methylation of the flagellin of Salmonella typhimurium. J. Bacteriol. 105:211-219.
    • (1971) J. Bacteriol. , vol.105 , pp. 211-219
    • Tronick, S.R.1    Martinez, R.J.2
  • 10
    • 33646757219 scopus 로고    scopus 로고
    • Flagellar glycosylation-a new component of the motility repertoire
    • Logan SM. 2006. Flagellar glycosylation-a new component of the motility repertoire? Microbiology 152:1249-1262.
    • (2006) Microbiology , vol.152 , pp. 1249-1262
    • Logan, S.M.1
  • 11
    • 35648945254 scopus 로고    scopus 로고
    • Campylobacter flagella: not just for motility
    • Guerry P. 2007. Campylobacter flagella: not just for motility. Trends Microbiol. 15:456-461.
    • (2007) Trends Microbiol. , vol.15 , pp. 456-461
    • Guerry, P.1
  • 12
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm M, Soo EC, Aubry AJ, Austin J, Thibault P, Logan SM. 2003. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol. Microbiol. 48:1579-1592.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 13
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: protein glycosylation in pathogenic bacteria
    • Benz I, Schmidt MA. 2002. Never say never again: protein glycosylation in pathogenic bacteria. Mol. Microbiol. 45:267-276.
    • (2002) Mol. Microbiol. , vol.45 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 14
  • 18
    • 0242575011 scopus 로고    scopus 로고
    • Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity
    • Takeuchi K, Taguchi F, Inagaki Y, Toyoda K, Shiraishi T, Ichinose Y. 2003. Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity. J. Bacteriol. 185:6658-6665.
    • (2003) J. Bacteriol. , vol.185 , pp. 6658-6665
    • Takeuchi, K.1    Taguchi, F.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 19
    • 1942540030 scopus 로고    scopus 로고
    • Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa
    • Schirm M, Arora SK, Verma A, Vinogradov E, Thibault P, Ramphal R, Logan SM. 2004. Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa. J. Bacteriol. 186:2523-2531.
    • (2004) J. Bacteriol. , vol.186 , pp. 2523-2531
    • Schirm, M.1    Arora, S.K.2    Verma, A.3    Vinogradov, E.4    Thibault, P.5    Ramphal, R.6    Logan, S.M.7
  • 21
    • 33644850378 scopus 로고    scopus 로고
    • Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
    • Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson Logan J-RSM. 2006. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281:723-732.
    • (2006) J. Biol. Chem. , vol.281 , pp. 723-732
    • Schoenhofen, I.C.1    McNally, D.J.2    Vinogradov, E.3    Whitfield, D.4    Young, N.M.5    Dick, S.6    Wakarchuk, W.W.7    Brisson Logan, J.-R.S.M.8
  • 22
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K, Maki-Yonekura S, Namba K. 2003. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 23
  • 24
    • 70350445517 scopus 로고    scopus 로고
    • Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176
    • Ewing CP, Andreishcheva E, Guerry P. 2009. Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176. J. Bacteriol. 191:7086-7093.
    • (2009) J. Bacteriol. , vol.191 , pp. 7086-7093
    • Ewing, C.P.1    Andreishcheva, E.2    Guerry, P.3
  • 25
    • 79952424076 scopus 로고    scopus 로고
    • Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography electron capture dissociation tandem mass spectrometry
    • Zampronio CG, Blackwell G, Penn CW, Cooper HJ. 2011. Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography electron capture dissociation tandem mass spectrometry. J. Proteome Res. 10:1238-1245.
    • (2011) J. Proteome Res. , vol.10 , pp. 1238-1245
    • Zampronio, C.G.1    Blackwell, G.2    Penn, C.W.3    Cooper, H.J.4
  • 27
    • 40249116849 scopus 로고    scopus 로고
    • Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses
    • doi:10.1186/1471-2164-9-42
    • Gao H, Wang X, Yang Z, Palzkill T, Zhou J. 2008. Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses. BMC Genomics 9:42. doi:10.1186/1471-2164-9-42.
    • (2008) BMC Genomics , vol.9 , pp. 42
    • Gao, H.1    Wang, X.2    Yang, Z.3    Palzkill, T.4    Zhou, J.5
  • 31
    • 84871119668 scopus 로고    scopus 로고
    • A Crp-dependent two-component system regulates nitrate and nitrite respiration in Shewanella oneidensis
    • doi:10.1371/journal.pone.0051643
    • Dong Y, Wang J, Fu H, Zhou G, Shi M, Gao H. 2012. A Crp-dependent two-component system regulates nitrate and nitrite respiration in Shewanella oneidensis. PLoS One 7:e51643. doi:10.1371/journal.pone.0051643.
    • (2012) PLoS One , vol.7 , pp. 51643
    • Dong, Y.1    Wang, J.2    Fu, H.3    Zhou, G.4    Shi, M.5    Gao, H.6
  • 32
    • 0036428656 scopus 로고    scopus 로고
    • Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins
    • Logan SM, Kelly JF, Thibault P, Ewing CP, Guerry P. 2002. Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins. Mol. Microbiol. 46:587-597.
    • (2002) Mol. Microbiol. , vol.46 , pp. 587-597
    • Logan, S.M.1    Kelly, J.F.2    Thibault, P.3    Ewing, C.P.4    Guerry, P.5
  • 33
    • 33748687970 scopus 로고    scopus 로고
    • Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction
    • Schoenhofen IC, McNally DJ, Brisson J-R, Logan SM. 2006. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16:8C-14C.
    • (2006) Glycobiology , vol.16 , pp. 8-14
    • Schoenhofen, I.C.1    McNally, D.J.2    Brisson, J.-R.3    Logan, S.M.4
  • 34
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related α-keto acids: an evolutionary perspective
    • Angata T, Varki A. 2002. Chemical diversity in the sialic acids and related α-keto acids: an evolutionary perspective. Chem. Rev. 102:439-470.
    • (2002) Chem. Rev. , vol.102 , pp. 439-470
    • Angata, T.1    Varki, A.2
  • 36
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon S, Kelly JF, Logan SM, Ewing CP, Guerry P. 2003. Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol. Microbiol. 50:659-671.
    • (2003) Mol. Microbiol. , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 37
    • 79960416730 scopus 로고    scopus 로고
    • Glycosylation regulates specific induction of rice immune responses by Acidovorax avenae flagellin
    • Hirai H, Takai R, Iwano M, Nakai M, Kondo M, Takayama S, Isogai A, Che F-S. 2011. Glycosylation regulates specific induction of rice immune responses by Acidovorax avenae flagellin. J. Biol. Chem. 286:25519-25530.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25519-25530
    • Hirai, H.1    Takai, R.2    Iwano, M.3    Nakai, M.4    Kondo, M.5    Takayama, S.6    Isogai, A.7    Che, F.-S.8
  • 38
    • 66249092413 scopus 로고    scopus 로고
    • The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors
    • Schoenhofen IC, Vinogradov E, Whitfield DM, Brisson Logan J-RSM. 2009. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19:715-725.
    • (2009) Glycobiology , vol.19 , pp. 715-725
    • Schoenhofen, I.C.1    Vinogradov, E.2    Whitfield, D.M.3    Brisson Logan, J.-R.S.M.4
  • 40
    • 84055199934 scopus 로고    scopus 로고
    • Identification of genes involved in the glycosylation of modified viosamine of flagellins in Pseudomonas syringae by mass spectrometry
    • Yamamoto M, Ohnishi-Kameyama M, Nguyen CL, Taguchi F, Chiku K, Ishii T, Ono H, Yoshida M, Ichinose Y. 2011. Identification of genes involved in the glycosylation of modified viosamine of flagellins in Pseudomonas syringae by mass spectrometry. Genes 2:788-803.
    • (2011) Genes , vol.2 , pp. 788-803
    • Yamamoto, M.1    Ohnishi-Kameyama, M.2    Nguyen, C.L.3    Taguchi, F.4    Chiku, K.5    Ishii, T.6    Ono, H.7    Yoshida, M.8    Ichinose, Y.9
  • 41
    • 4944261230 scopus 로고    scopus 로고
    • Flagellin from Listeria monocytogenes is glycosylated with β-Olinked N-acetylglucosamine
    • Schirm M, Kalmokoff M, Aubry A, Thibault P, Sandoz M, Logan SM. 2004. Flagellin from Listeria monocytogenes is glycosylated with β-Olinked N-acetylglucosamine. J. Bacteriol. 186:6721-6727.
    • (2004) J. Bacteriol. , vol.186 , pp. 6721-6727
    • Schirm, M.1    Kalmokoff, M.2    Aubry, A.3    Thibault, P.4    Sandoz, M.5    Logan, S.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.